Solute carrier family 2, facilitated glucose transporter member 3 (SLC2A3)
The protein contains 496 amino acids for an estimated molecular weight of 53924 Da.
Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:9477959, PubMed:26176916). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate (PubMed:9477959, PubMed:26176916). Does not mediate fructose transport (PubMed:9477959, PubMed:26176916). (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs17728193 |
Biological Process
Carbohydrate metabolic process
Glucose import across plasma membrane
Glucose transmembrane transport
Glucose transport
Hexose transport
L-ascorbic acid metabolic process
Neutrophil degranulation
Pathogenesis
Small molecule metabolic process
Transmembrane transport
Transport across blood-brain barrier
Vitamin metabolic process
Water-soluble vitamin metabolic process
The reference OMIM entry for this protein is 138170
Solute carrier family 2 (facilitated glucose transporter), member 3; slc2a3
Glucose transporter 3; glut3
Glucose transporter, fetal skeletal muscle solute carrier family 2, member 3 pseudogene, included; slc2a3p, included
Glucose transporter 3
CLONING
The mRNA levels encoding glucose transporter (see SLC2A1; 138140 and SLC2A2; 138160) are very low in skeletal muscle, an important site of peripheral glucose uptake and utilization, suggesting that another protein may be responsible for glucose uptake by this tissue. Reasoning that there might be a family of structurally related glucose transport proteins in mammalian cells, just as there is a family of related proteins involved in sugar and nutrient uptake in Escherichia coli, Kayano et al. (1988) screened a human fetal skeletal muscle cDNA library using low-stringency conditions to identify clones that cross-hybridize with a hepatoma-derived glucose transporter cDNA. The mRNA encoding this protein was present in most if not all tissues, although the amounts varied widely. The 496-amino acid fetal muscle glucose transporter-like protein shares 64.4% and 51.6% identity with the previously described GLUT1 (138140) and GLUT2 (138160) sequences, respectively. - PSEUDOGENE By the homology screening approach, Kayano et al. (1990) identified a glucose transporter-like transcript, called GLUT6 by them, with an apparently ubiquitous tissue distribution. Sequence analysis of a cDNA clone for this transcript revealed a high level of base identity (79.6%) with GLUT3. However, the cDNA was found to contain multiple stop codons and frameshifts, indicating that it probably does not encode a functional glucose transporter. The extensive identity of the GLUT6 cDNA with the GLUT3 cDNA sequence suggested that the GLUT-like region of the GLUT6 transcript may have arisen by the insertion of a reverse-transcribed copy of GLUT3 into the noncoding region of a ubiquitously expressed gene--a 'hitchhiking' phenomenon. (This pseudogene is also symbolized SLC2A3P and GLUT3P1.)GENE FUNCTION
Gould and Holman (1993), who provided a review of the glucose transporter family, referred to GLUT3 as the brain-type glucose transporter. It appears that high GLUT3 protein expression is confined generally to tissues that exhibit a high glucose demand, such as brain and nerve. Hauguel-de Mouzon et al. (1997) examined the cellular localization of GLUT3 mRNA and protein. In situ hybridization showed that GLUT3 mRNA was present in the trophoblast cell layer and in vascular endothelium with a heterogeneous distribution pattern. GLUT3 protein, migrating at an apparent molecular mass of 49 kD, was detected by immunoblotting in membranes from whole placenta and endothelial cells derived from intraplacental microvessels, but not in isolated trophoblast cells. This cell-specific pattern of expression was confirmed by immunocytochemical studies showing localization of GLUT3 protein in vascular endothelium. Based on the cell-specific distribution of GLUT3 protein at the fetal interface, the authors suggested that this protein may be important in the transport of glucose from the placenta to the fetal circulation.MAPPING
By in situ hybridization to metaphase chromosomes, Kayano et al. (1988) assigned the gene encoding this protein to 12p13.3. - PSEUDOGENE By hybridization of a cDNA probe to a panel of somatic cell hybrids and by in situ hybridization, Fan et al. (1989) showed that the GLUT3 pseudogene GLUT6 is located on chromosome 5. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 138170 was added.